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Volumn 7, Issue 3, 2012, Pages 369-381

Post-translational modifications of host proteins by Legionella pneumophila: A sophisticated survival strategy

Author keywords

bacterial effector; host signaling pathway; Legionella pneumophila; post translational modification

Indexed keywords

BACTERIAL PROTEIN; UBIQUITIN;

EID: 84858049415     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.12.9     Document Type: Review
Times cited : (26)

References (109)
  • 1
    • 0017726281 scopus 로고
    • Legionnaires' disease: Description of an epidemic of pneumonia
    • Fraser DW, Tsai TR, Orenstein W et al. Legionnaires' disease: description of an epidemic of pneumonia. N. Engl. J. Med. 297(22), 1189-1197 (1977).
    • (1977) N. Engl. J. Med. , vol.297 , Issue.22 , pp. 1189-1197
    • Fraser, D.W.1    Tsai, T.R.2    Orenstein, W.3
  • 2
    • 0018885613 scopus 로고
    • Legionnaires' disease bacterium (Legionella pneumophila) multiples intracellularly in human monocytes
    • Horwitz MA, Silverstein SC. Legionnaires' disease bacterium (Legionella pneumophila) multiples intracellularly in human monocytes. J. Clin. Invest. 66(3), 441-450 (1980).
    • (1980) J. Clin. Invest. , vol.66 , Issue.3 , pp. 441-450
    • Horwitz, M.A.1    Silverstein, S.C.2
  • 3
    • 0021169749 scopus 로고
    • Interaction between the Legionnaires' disease bacterium (Legionella pneumophila) and human alveolar macrophages. Influence of antibody, lymphokines, and hydrocortisone
    • Nash TW, Libby DM, Horwitz MA. Interaction between the Legionnaires' disease bacterium (Legionella pneumophila) and human alveolar macrophages. Influence of antibody, lymphokines, and hydrocortisone. J. Clin. Invest. 74(3), 771-782 (1984).
    • (1984) J. Clin. Invest. , vol.74 , Issue.3 , pp. 771-782
    • Nash, T.W.1    Libby, D.M.2    Horwitz, M.A.3
  • 4
    • 0019254065 scopus 로고
    • Preliminary report on the pathogenicity of Legionella pneumophila for freshwater and soil amoebae
    • Rowbotham TJ. Preliminary report on the pathogenicity of Legionella pneumophila for freshwater and soil amoebae. J. Clin. Pathol. 33(12), 1179-1183 (1980).
    • (1980) J. Clin. Pathol. , vol.33 , Issue.12 , pp. 1179-1183
    • Rowbotham, T.J.1
  • 5
    • 0032539674 scopus 로고    scopus 로고
    • Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome
    • Segal G, Purcell M, Shuman HA. Host cell killing and bacterial conjugation require overlapping sets of genes within a 22-kb region of the Legionella pneumophila genome. Proc. Natl Acad. Sci. USA 95(4), 1669-1674 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , Issue.4 , pp. 1669-1674
    • Segal, G.1    Purcell, M.2    Shuman, H.A.3
  • 6
    • 0032932436 scopus 로고    scopus 로고
    • Legionella pneumophila utilizes the same genes to multiply within Acanthamoeba castellanii and human macrophages
    • Segal G, Shuman HA. Legionella pneumophila utilizes the same genes to multiply within Acanthamoeba castellanii and human macrophages. Infect. Immun. 67(5), 2117-2124 (1999).
    • (1999) Infect. Immun. , vol.67 , Issue.5 , pp. 2117-2124
    • Segal, G.1    Shuman, H.A.2
  • 7
    • 0032488861 scopus 로고    scopus 로고
    • Conjugative transfer by the virulence system of Legionella pneumophila
    • Vogel JP, Andrews HL, Wong SK, Isberg RR. Conjugative transfer by the virulence system of Legionella pneumophila. Science 279(5352), 873-876 (1998).
    • (1998) Science , vol.279 , Issue.5352 , pp. 873-876
    • Vogel, J.P.1    Andrews, H.L.2    Wong, S.K.3    Isberg, R.R.4
  • 8
    • 0027472133 scopus 로고
    • Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila
    • Berger KH, Isberg RR. Two distinct defects in intracellular growth complemented by a single genetic locus in Legionella pneumophila. Mol. Microbiol. 7(1), 7-19 (1993).
    • (1993) Mol. Microbiol. , vol.7 , Issue.1 , pp. 7-19
    • Berger, K.H.1    Isberg, R.R.2
  • 9
    • 0026738809 scopus 로고
    • Identification of a Legionella pneumophila locus required for intracellular multiplication in human macrophages
    • Marra A, Blander SJ, Horwitz MA, Shuman HA. Identification of a Legionella pneumophila locus required for intracellular multiplication in human macrophages. Proc. Natl Acad. Sci. USA 89(20), 9607-9611 (1992).
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , Issue.20 , pp. 9607-9611
    • Marra, A.1    Blander, S.J.2    Horwitz, M.A.3    Shuman, H.A.4
  • 10
    • 70049110355 scopus 로고    scopus 로고
    • Genome-scale identification of Legionella pneumophila effectors using a machine learning approach
    • Employed a new bioinformatics approach based on machine learning to identify secreted subtstrates of the Dot/Icm type IV secretion system
    • Burstein D, Zusman T, Degtyar E, Viner R, Segal G, Pupko T. Genome-scale identification of Legionella pneumophila effectors using a machine learning approach. PLoS Pathog. 5(7), E1000508 (2009). Employed a new bioinformatics approach based on machine learning to identify secreted subtstrates of the Dot/Icm type IV secretion system.
    • (2009) PLoS Pathog. , vol.5 , Issue.7
    • Burstein, D.1    Zusman, T.2    Degtyar, E.3    Viner, R.4    Segal, G.5    Pupko, T.6
  • 11
    • 18444408390 scopus 로고    scopus 로고
    • A yeast genetic system for the identification and characterization of substrate proteins transferred into host cells by the Legionella pneumophila Dot/Icm system
    • Reported a random screening assay to identify bacterial proteins that conferred a conditional growth defect in yeast
    • Campodonico EM, Chesnel L, Roy CR. A yeast genetic system for the identification and characterization of substrate proteins transferred into host cells by the Legionella pneumophila Dot/Icm system. Mol. Microbiol. 56(4), 918-933 (2005). Reported a random screening assay to identify bacterial proteins that conferred a conditional growth defect in yeast.
    • (2005) Mol. Microbiol. , vol.56 , Issue.4 , pp. 918-933
    • Campodonico, E.M.1    Chesnel, L.2    Roy, C.R.3
  • 12
    • 50849115482 scopus 로고    scopus 로고
    • Legionella eukaryotic-like type IV substrates interfere with organelle trafficking
    • De Felipe KS, Glover RT, Charpentier X et al. Legionella eukaryotic-like type IV substrates interfere with organelle trafficking. PLoS Pathog. 4(8), E1000117 (2008).
    • (2008) PLoS Pathog. , vol.4 , Issue.8
    • De Felipe, K.S.1    Glover, R.T.2    Charpentier, X.3
  • 13
    • 27744546297 scopus 로고    scopus 로고
    • Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer
    • Used for the first time a fluorescence-based translocation assay to identify Dot/Icm secreted substrates
    • De Felipe KS, Pampou S, Jovanovic OS et al. Evidence for acquisition of Legionella type IV secretion substrates via interdomain horizontal gene transfer. J. Bacteriol. 187(22), 7716-7726 (2005). Used for the first time a fluorescence-based translocation assay to identify Dot/Icm secreted substrates.
    • (2005) J. Bacteriol. , vol.187 , Issue.22 , pp. 7716-7726
    • De Felipe, K.S.1    Pampou, S.2    Jovanovic, O.S.3
  • 14
    • 58349107899 scopus 로고    scopus 로고
    • Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways
    • Heidtman M, Chen EJ, Moy MY, Isberg RR. Large-scale identification of Legionella pneumophila Dot/Icm substrates that modulate host cell vesicle trafficking pathways. Cell. Microbiol. 11(2), 230-248 (2009).
    • (2009) Cell. Microbiol. , vol.11 , Issue.2 , pp. 230-248
    • Heidtman, M.1    Chen, E.J.2    Moy, M.Y.3    Isberg, R.R.4
  • 15
    • 16344374697 scopus 로고    scopus 로고
    • Pathogen effector protein screening in yeast identifies Legionella factors that interfere with membrane trafficking
    • Utilized for the first time effector protein screening in yeast to identify bacterial proteins that produced membrane trafficking defects in yeast
    • Shohdy N, Efe JA, Emr SD, Shuman HA. Pathogen effector protein screening in yeast identifies Legionella factors that interfere with membrane trafficking. Proc. Natl Acad. Sci. USA 102(13), 4866-4871 (2005). Utilized for the first time effector protein screening in yeast to identify bacterial proteins that produced membrane trafficking defects in yeast.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.13 , pp. 4866-4871
    • Shohdy, N.1    Efe, J.A.2    Emr, S.D.3    Shuman, H.A.4
  • 16
    • 79952403625 scopus 로고    scopus 로고
    • Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila
    • Zhu W, Banga S, Tan Y et al. Comprehensive identification of protein substrates of the Dot/Icm type IV transporter of Legionella pneumophila. PLoS One 6(3), E17638 (2011).
    • (2011) PLoS One , vol.6 , Issue.3
    • Zhu, W.1    Banga, S.2    Tan, Y.3
  • 17
    • 10044263696 scopus 로고    scopus 로고
    • Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity
    • Cazalet C, Rusniok C, Bruggemann H et al. Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity. Nat. Genet. 36(11), 1165-1173 (2004).
    • (2004) Nat. Genet. , vol.36 , Issue.11 , pp. 1165-1173
    • Cazalet, C.1    Rusniok, C.2    Bruggemann, H.3
  • 18
    • 4644276577 scopus 로고    scopus 로고
    • The genomic sequence of the accidental pathogen Legionella pneumophila
    • Chien M, Morozova I, Shi S et al. The genomic sequence of the accidental pathogen Legionella pneumophila. Science 305(5692), 1966-1968 (2004).
    • (2004) Science , vol.305 , Issue.5692 , pp. 1966-1968
    • Chien, M.1    Morozova, I.2    Shi, S.3
  • 19
    • 67649388172 scopus 로고    scopus 로고
    • From pathogenesis to cell biology and back
    • Mostowy S, Cossart P. From pathogenesis to cell biology and back. Cell Host Microbe 5(6), 510-513 (2009).
    • (2009) Cell Host Microbe , vol.5 , Issue.6 , pp. 510-513
    • Mostowy, S.1    Cossart, P.2
  • 20
    • 78049370513 scopus 로고    scopus 로고
    • Modulation of host cell function by Legionella pneumophila type IV effectors
    • Hubber A, Roy CR. Modulation of host cell function by Legionella pneumophila type IV effectors. Annu. Rev. Cell. Dev. Biol. 26, 261-283 (2010).
    • (2010) Annu. Rev. Cell. Dev. Biol. , vol.26 , pp. 261-283
    • Hubber, A.1    Roy, C.R.2
  • 21
    • 57649149094 scopus 로고    scopus 로고
    • The Legionella pneumophila replication vacuole: Making a cosy niche inside host cells
    • Isberg RR, O'Connor TJ, Heidtman M. The Legionella pneumophila replication vacuole: making a cosy niche inside host cells. Nat. Rev. Microbiol. 7(1), 13-24 (2009).
    • (2009) Nat. Rev. Microbiol. , vol.7 , Issue.1 , pp. 13-24
    • Isberg, R.R.1    O'Connor, T.J.2    Heidtman, M.3
  • 22
    • 69849087003 scopus 로고    scopus 로고
    • Molecular mimicry: An important virulence strategy employed by Legionella pneumophila to subvert host functions
    • Nora T, Lomma M, Gomez-Valero L, Buchrieser C. Molecular mimicry: an important virulence strategy employed by Legionella pneumophila to subvert host functions. Future Microbiol. 4, 691-701 (2009).
    • (2009) Future Microbiol. , vol.4 , pp. 691-701
    • Nora, T.1    Lomma, M.2    Gomez-Valero, L.3    Buchrieser, C.4
  • 23
    • 33745800293 scopus 로고    scopus 로고
    • Interpreting the protein language using proteomics
    • Jensen ON. Interpreting the protein language using proteomics. Nat. Rev. Mol. Cell. Biol. 7(6), 391-403 (2006).
    • (2006) Nat. Rev. Mol. Cell. Biol. , vol.7 , Issue.6 , pp. 391-403
    • Jensen, O.N.1
  • 24
    • 78650153662 scopus 로고    scopus 로고
    • Pathogen-mediated posttranslational modifications: A re-emerging field
    • Up-to-date review on how different bacterial pathogens may modulate host functions through post-translational modifications
    • Ribet D, Cossart P. Pathogen-mediated posttranslational modifications: a re-emerging field. Cell 143(5), 694-702 (2011). Up-to-date review on how different bacterial pathogens may modulate host functions through post-translational modifications.
    • (2011) Cell , vol.143 , Issue.5 , pp. 694-702
    • Ribet, D.1    Cossart, P.2
  • 25
    • 65649115267 scopus 로고    scopus 로고
    • Recognition and processing of ubiquitin-protein conjugates by the proteasome
    • Finley D. Recognition and processing of ubiquitin-protein conjugates by the proteasome. Annu. Rev. Biochem. 78, 477-513 (2009).
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 477-513
    • Finley, D.1
  • 26
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart CM, Cohen RE. Proteasomes and their kin: proteases in the machine age. Nat. Rev. Mol. Cell. Biol. 5(3), 177-187 (2004).
    • (2004) Nat. Rev. Mol. Cell. Biol. , vol.5 , Issue.3 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 27
    • 78650100616 scopus 로고    scopus 로고
    • Ubiquitin: Same molecule, different degradation pathways
    • Clague MJ, Urbé S. Ubiquitin: same molecule, different degradation pathways. Cell 143(5), 682-685 (2010).
    • (2010) Cell , vol.143 , Issue.5 , pp. 682-685
    • Clague, M.J.1    Urbé, S.2
  • 28
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • Pickart CM, Fushman D. Polyubiquitin chains: polymeric protein signals. Curr. Opin. Chem. Biol. 8(6), 610-616 (2004).
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 29
    • 0035292759 scopus 로고    scopus 로고
    • Themes and variations on ubiquitylation
    • Weissman AM. Themes and variations on ubiquitylation. Nat. Rev. Mol. Cell. Biol. 2(3), 169-178 (2001).
    • (2001) Nat. Rev. Mol. Cell. Biol. , vol.2 , Issue.3 , pp. 169-178
    • Weissman, A.M.1
  • 30
    • 47549111312 scopus 로고    scopus 로고
    • Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes
    • Lee I, Schindelin H. Structural insights into E1-catalyzed ubiquitin activation and transfer to conjugating enzymes. Cell 134(2), 268-278 (2008).
    • (2008) Cell , vol.134 , Issue.2 , pp. 268-278
    • Lee, I.1    Schindelin, H.2
  • 31
    • 77951651753 scopus 로고    scopus 로고
    • The family of ubiquitin-conjugating enzymes (E2s): Deciding between life and death of proteins
    • Van Wijk SJ, Timmers HT. The family of ubiquitin-conjugating enzymes (E2s): deciding between life and death of proteins. FASEB J. 24(4), 981-993 (2010).
    • (2010) FASEB J. , vol.24 , Issue.4 , pp. 981-993
    • Van Wijk, S.J.1    Timmers, H.T.2
  • 33
    • 77649328287 scopus 로고    scopus 로고
    • Animal HECT ubiquitin ligases: Evolution and functional implications
    • Marín I. Animal HECT ubiquitin ligases: evolution and functional implications. BMC Evol. Biol. 10, 56 (2010).
    • (2010) BMC Evol. Biol. , vol.10 , pp. 56
    • Marín, I.1
  • 34
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D, Kumar S. Physiological functions of the HECT family of ubiquitin ligases. Nat. Rev. Mol. Cell. Biol. 10(6), 398-409 (2009).
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , Issue.6 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 37
    • 68049084674 scopus 로고    scopus 로고
    • Breaking the chains: Structure and function of the deubiquitinases
    • Komander D, Clague MJ, Urbe S. Breaking the chains: structure and function of the deubiquitinases. Nat. Rev. Mol. Cell. Biol. 10, 550-563 (2009).
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 550-563
    • Komander, D.1    Clague, M.J.2    Urbe, S.3
  • 38
    • 33947714944 scopus 로고    scopus 로고
    • Bacterial interference of ubiquitination and deubiquitination
    • Rytkonen A, Holden DW. Bacterial interference of ubiquitination and deubiquitination. Cell Host Microbe 1(1), 13-22 (2007).
    • (2007) Cell Host Microbe , vol.1 , Issue.1 , pp. 13-22
    • Rytkonen, A.1    Holden, D.W.2
  • 39
    • 33750034105 scopus 로고    scopus 로고
    • The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase
    • Zhang Y, Higashide WM, McCormick BA, Chen J, Zhou D. The inflammation-associated Salmonella SopA is a HECT-like E3 ubiquitin ligase. Mol. Microbiol. 62(3), 786-793 (2006).
    • (2006) Mol. Microbiol. , vol.62 , Issue.3 , pp. 786-793
    • Zhang, Y.1    Higashide, W.M.2    McCormick, B.A.3    Chen, J.4    Zhou, D.5
  • 41
    • 44449107633 scopus 로고    scopus 로고
    • Salmonella secreted factor L deubiquitinase of Salmonella typhimurium inhibits NF-kappaB, suppresses IkappaBalpha ubiquitination and modulates innate immune responses
    • Le Negrate G, Faustin B, Welsh K et al. Salmonella secreted factor L deubiquitinase of Salmonella typhimurium inhibits NF-kappaB, suppresses IkappaBalpha ubiquitination and modulates innate immune responses. J. Immunol. 80(7), 5045-5056 (2008).
    • (2008) J. Immunol. , vol.80 , Issue.7 , pp. 5045-5056
    • Le Negrate, G.1    Faustin, B.2    Welsh, K.3
  • 42
    • 39849096721 scopus 로고    scopus 로고
    • Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions
    • Kubori T, Hyakutake A, Nagai H. Legionella translocates an E3 ubiquitin ligase that has multiple U-boxes with distinct functions. Mol. Microbiol. 67(6), 1307-1319 (2008).
    • (2008) Mol. Microbiol. , vol.67 , Issue.6 , pp. 1307-1319
    • Kubori, T.1    Hyakutake, A.2    Nagai, H.3
  • 43
    • 78651234971 scopus 로고    scopus 로고
    • Legionella metaeffector exploits host proteasome to temporally regulate cognate effector
    • Demonstrates for the first time that a bacterial effector can regulate the activity of another bacterial effector in the host cell
    • Kubori T, Shinzawa N, Kanuka H, Nagai H. Legionella metaeffector exploits host proteasome to temporally regulate cognate effector. PLoS Pathog. 6(12), E1001216 (2010). Demonstrates for the first time that a bacterial effector can regulate the activity of another bacterial effector in the host cell.
    • (2010) PLoS Pathog. , vol.6 , Issue.12
    • Kubori, T.1    Shinzawa, N.2    Kanuka, H.3    Nagai, H.4
  • 45
    • 0030695025 scopus 로고    scopus 로고
    • A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p
    • Feldman RM, Correll CC, Kaplan KB, Deshaies RJ. A complex of Cdc4p, Skp1p, and Cdc53p/cullin catalyzes ubiquitination of the phosphorylated CDK inhibitor Sic1p. Cell 91(2), 221-230 (1997).
    • (1997) Cell , vol.91 , Issue.2 , pp. 221-230
    • Feldman, R.M.1    Correll, C.C.2    Kaplan, K.B.3    Deshaies, R.J.4
  • 46
    • 0030662523 scopus 로고    scopus 로고
    • F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex
    • Skowyra D, Craig KL, Tyers M, Elledge SJ, Harper JW. F-box proteins are receptors that recruit phosphorylated substrates to the SCF ubiquitin-ligase complex. Cell 91(2), 209-219 (1997).
    • (1997) Cell , vol.91 , Issue.2 , pp. 209-219
    • Skowyra, D.1    Craig, K.L.2    Tyers, M.3    Elledge, S.J.4    Harper, J.W.5
  • 48
    • 67549093540 scopus 로고    scopus 로고
    • SnapShot: F box proteins I
    • Skaar JR, Pagan JK, Pagano M. SnapShot: F box proteins I. Cell 137(6), 1160.E1 (2009).
    • (2009) Cell , vol.137 , Issue.6
    • Skaar, J.R.1    Pagan, J.K.2    Pagano, M.3
  • 49
    • 33846574355 scopus 로고    scopus 로고
    • Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems
    • Comprehensive review on how different bacterial pathogens exploit the host ubiquitin pathways
    • Angot A, Vergunst A, Genin S, Peeters N. Exploitation of eukaryotic ubiquitin signaling pathways by effectors translocated by bacterial type III and type IV secretion systems. PLoS Pathog. 3(1), E3 (2007). Comprehensive review on how different bacterial pathogens exploit the host ubiquitin pathways.
    • (2007) PLoS Pathog. , vol.3 , Issue.1
    • Angot, A.1    Vergunst, A.2    Genin, S.3    Peeters, N.4
  • 50
    • 33646234683 scopus 로고    scopus 로고
    • RNA interference analysis of Legionella in Drosophila cells: Exploitation of early secretory apparatus dynamics
    • Dorer MS, Kirton D, Bader JS, Isberg RR. RNA interference analysis of Legionella in Drosophila cells: exploitation of early secretory apparatus dynamics. PLoS Pathog. 2(4), E34 (2006).
    • (2006) PLoS Pathog. , vol.2 , Issue.4
    • Dorer, M.S.1    Kirton, D.2    Bader, J.S.3    Isberg, R.R.4
  • 51
    • 54249166663 scopus 로고    scopus 로고
    • Dot/Icm-translocated ankyrin protein of Legionella pneumophila is required for intracellular proliferation within human macrophages and protozoa
    • Al-Khodor S, Price CT, Habyarimana F, Kalia A, Abu Kwaik Y. A Dot/Icm-translocated ankyrin protein of Legionella pneumophila is required for intracellular proliferation within human macrophages and protozoa. Mol. Microbiol. 70(4), 908-923 (2008).
    • (2008) Mol. Microbiol. , vol.70 , Issue.4 , pp. 908-923
    • Al-Khodor, S.1    Price, C.T.2    Habyarimana, F.3    Kalia, A.4    Abu Kwaik, Y.A.5
  • 52
    • 77953704524 scopus 로고    scopus 로고
    • The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication
    • Lomma M, Dervins-Ravault D, Rolando M et al. The Legionella pneumophila F-box protein Lpp2082 (AnkB) modulates ubiquitination of the host protein parvin B and promotes intracellular replication. Cell. Microbiol. 12(9), 1272-1291 (2010).
    • (2010) Cell. Microbiol. , vol.12 , Issue.9 , pp. 1272-1291
    • Lomma, M.1    Dervins-Ravault, D.2    Rolando, M.3
  • 53
    • 74549200971 scopus 로고    scopus 로고
    • Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa
    • Price CT, Al-Khodor S, Al-Quadan T et al. Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa. PLoS Pathog. 5(12), E1000704 (2009).
    • (2009) PLoS Pathog. , vol.5 , Issue.12
    • Price, C.T.1    Al-Khodor, S.2    Al-Quadan, T.3
  • 54
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily
    • Olski TM, Noegel AA, Korenbaum E. Parvin, a 42 kDa focal adhesion protein, related to the alpha-actinin superfamily. J. Cell Sci. 114(Pt 3), 525-538 (2001).
    • (2001) J. Cell Sci. , vol.114 , Issue.PART 3 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 55
    • 0035844879 scopus 로고    scopus 로고
    • A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction
    • Yamaji S, Suzuki A, Sugiyama Y et al. A novel integrin-linked kinase-binding protein, affixin, is involved in the early stage of cell-substrate interaction. J. Cell Biol. 153(6), 1251-1264 (2001).
    • (2001) J. Cell Biol. , vol.153 , Issue.6 , pp. 1251-1264
    • Yamaji, S.1    Suzuki, A.2    Sugiyama, Y.3
  • 57
    • 77956644100 scopus 로고    scopus 로고
    • E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates
    • Ensminger AW, Isberg RR. E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates. Infect. Immun. 78(9), 3905-3919 (2010).
    • (2010) Infect. Immun. , vol.78 , Issue.9 , pp. 3905-3919
    • Ensminger, A.W.1    Isberg, R.R.2
  • 58
    • 58349085112 scopus 로고    scopus 로고
    • Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system
    • Ivanov SS, Roy CR. Modulation of ubiquitin dynamics and suppression of DALIS formation by the Legionella pneumophila Dot/Icm system. Cell. Microbiol. 11(2), 261-278 (2009).
    • (2009) Cell. Microbiol. , vol.11 , Issue.2 , pp. 261-278
    • Ivanov, S.S.1    Roy, C.R.2
  • 59
    • 14044263586 scopus 로고    scopus 로고
    • Cutting edge: Microbial products elicit formation of dendritic cell aggresome-like induced structures in macrophages
    • Canadien V, Tan T, Zilber R, Szeto J, Perrin AJ, Brumell JH. Cutting edge: microbial products elicit formation of dendritic cell aggresome-like induced structures in macrophages. J. Immunol. 174(5), 2471-2475 (2005).
    • (2005) J. Immunol. , vol.174 , Issue.5 , pp. 2471-2475
    • Canadien, V.1    Tan, T.2    Zilber, R.3    Szeto, J.4    Perrin, A.J.5    Brumell, J.H.6
  • 60
    • 78049354410 scopus 로고    scopus 로고
    • Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins
    • First description showing that a bacterial effector can exploit the host prenylation (farnesylation) machinery
    • Ivanov SS, Charron G, Hang HC, Roy CR. Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins. J. Biol. Chem. 285(45), 34686-34698 (2010). First description showing that a bacterial effector can exploit the host prenylation (farnesylation) machinery.
    • (2010) J. Biol. Chem. , vol.285 , Issue.45 , pp. 34686-34698
    • Ivanov, S.S.1    Charron, G.2    Hang, H.C.3    Roy, C.R.4
  • 61
    • 77955397296 scopus 로고    scopus 로고
    • Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila
    • First description showing that a bacterial effector can exploit the host prenylation (farnesylation) machinery
    • Price CT, Al-Quadan T, Santic M, Jones SC, Abu Kwaik Y. Exploitation of conserved eukaryotic host cell farnesylation machinery by an F-box effector of Legionella pneumophila. J. Exp. Med. 207(8), 1713-1726 (2010). First description showing that a bacterial effector can exploit the host prenylation (farnesylation) machinery.
    • (2010) J. Exp. Med. , vol.207 , Issue.8 , pp. 1713-1726
    • Price, C.T.1    Al-Quadan, T.2    Santic, M.3    Jones, S.C.4    Abu Kwaik, Y.5
  • 62
    • 33646777423 scopus 로고    scopus 로고
    • Thematic review series: Lipid posttranslational modifications. CAAX modification and membrane targeting of Ras
    • Wright LP, Philips MR. Thematic review series: lipid posttranslational modifications. CAAX modification and membrane targeting of Ras. J. Lipid Res. 47(5), 883-891 (2006).
    • (2006) J. Lipid Res. , vol.47 , Issue.5 , pp. 883-891
    • Wright, L.P.1    Philips, M.R.2
  • 63
    • 82355191738 scopus 로고    scopus 로고
    • Anchoring of bacterial effectors to host membranes through host-mediated lipidation by prenylation: A common paradigm
    • Al-Quadan T, Price CT, London N, Schueler-Furman O, Abu Kwaik Y. Anchoring of bacterial effectors to host membranes through host-mediated lipidation by prenylation: a common paradigm. Trends Microbiol. 19(12), 573-579 (2011).
    • (2011) Trends Microbiol. , vol.19 , Issue.12 , pp. 573-579
    • Al-Quadan, T.1    Price, C.T.2    London, N.3    Schueler-Furman, O.4    Abu Kwaik, Y.5
  • 64
    • 80055093214 scopus 로고    scopus 로고
    • Host-mediated post-translational prenylation of novel Dot/Icm-translocated effectors of Legionella pneumophila
    • Price CT, Jones SC, Amundson KE, Kwaik YA. Host-mediated post-translational prenylation of novel Dot/Icm-translocated effectors of Legionella pneumophila. Front. Microbiol. 1, 131 (2010).
    • (2010) Front. Microbiol. , vol.1 , pp. 131
    • Price, C.T.1    Jones, S.C.2    Amundson, K.E.3    Kwaik, Y.A.4
  • 65
    • 80855133900 scopus 로고    scopus 로고
    • Exploitation of host polyubiquitination machinery through molecular mimicry by eukaryotic-like bacterial F-Box effectors
    • Price CT, Kwaik YA. Exploitation of host polyubiquitination machinery through molecular mimicry by eukaryotic-like bacterial F-Box effectors. Front. Microbiol. 1, 122 (2010).
    • (2010) Front. Microbiol. , vol.1 , pp. 122
    • Price, C.T.1    Kwaik, Y.A.2
  • 66
    • 83855160757 scopus 로고    scopus 로고
    • Host proteasomal degradation generates amino acids essential for intracellular bacterial growth
    • Price CT, Al-Quadan T, Santic M, Rosenshine I, Abu Kwaik Y. Host proteasomal degradation generates amino acids essential for intracellular bacterial growth. Science 334(6062), 1553-1557 (2011).
    • (2011) Science , vol.334 , Issue.6062 , pp. 1553-1557
    • Price, C.T.1    Al-Quadan, T.2    Santic, M.3    Rosenshine, I.4    Abu Kwaik, Y.5
  • 67
    • 0028838971 scopus 로고
    • Protein kinases and phosphatases: The yin and yang of protein phosphorylation and signaling
    • Hunter T. Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling. Cell 80(2), 225-236 (1995).
    • (1995) Cell , vol.80 , Issue.2 , pp. 225-236
    • Hunter, T.1
  • 68
    • 0034662928 scopus 로고    scopus 로고
    • A distinctive role for the Yersinia protein kinase: Actin binding, kinase activation, and cytoskeleton disruption
    • Juris SJ, Rudolph AE, Huddler D, Orth K, Dixon JE. A distinctive role for the Yersinia protein kinase: actin binding, kinase activation, and cytoskeleton disruption. Proc. Natl Acad. Sci. USA 97(17), 9431-9436 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.17 , pp. 9431-9436
    • Juris, S.J.1    Rudolph, A.E.2    Huddler, D.3    Orth, K.4    Dixon, J.E.5
  • 69
    • 29344445221 scopus 로고    scopus 로고
    • Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry
    • Juris SJ, Shah K, Shokat K, Dixon JE, Vacratsis PO. Identification of otubain 1 as a novel substrate for the Yersinia protein kinase using chemical genetics and mass spectrometry. FEBS Lett. 580(1), 179-183 (2006).
    • (2006) FEBS Lett. , vol.580 , Issue.1 , pp. 179-183
    • Juris, S.J.1    Shah, K.2    Shokat, K.3    Dixon, J.E.4    Vacratsis, P.O.5
  • 70
    • 81255205278 scopus 로고    scopus 로고
    • Extensive recombination events and horizontal gene transfer shaped the Legionella pneumophila genomes
    • Gomez-Valero L, Rusniok C, Jarraud S et al. Extensive recombination events and horizontal gene transfer shaped the Legionella pneumophila genomes. BMC Genomics 12, 536 (2011).
    • (2011) BMC Genomics , vol.12 , pp. 536
    • Gomez-Valero, L.1    Rusniok, C.2    Jarraud, S.3
  • 71
    • 69549133937 scopus 로고    scopus 로고
    • A Legionella type IV effector activates the NF-kappaB pathway by phosphorylating the IkappaB family of inhibitors
    • Ge J, Xu H, Li T et al. A Legionella type IV effector activates the NF-kappaB pathway by phosphorylating the IkappaB family of inhibitors. Proc. Natl Acad. Sci. USA 106(33), 13725-13730 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.33 , pp. 13725-13730
    • Ge, J.1    Xu, H.2    Li, T.3
  • 72
    • 0036009115 scopus 로고    scopus 로고
    • NF-kappaB at the crossroads of life and death
    • Karin M, Lin A. NF-kappaB at the crossroads of life and death. Nat. Immunol. 3(3), 221-227 (2002).
    • (2002) Nat. Immunol. , vol.3 , Issue.3 , pp. 221-227
    • Karin, M.1    Lin, A.2
  • 73
    • 72749121799 scopus 로고    scopus 로고
    • Temporal resolution of two-tracked NF-kappaB activation by Legionella pneumophila
    • Bartfeld S, Engels C, Bauer B et al. Temporal resolution of two-tracked NF-kappaB activation by Legionella pneumophila. Cell. Microbiol. 11(11), 1638-1651 (2009).
    • (2009) Cell. Microbiol. , vol.11 , Issue.11 , pp. 1638-1651
    • Bartfeld, S.1    Engels, C.2    Bauer, B.3
  • 74
    • 77957137443 scopus 로고    scopus 로고
    • LnaB: A Legionella pneumophila activator of NF-kappaB
    • Losick VP, Haenssler E, Moy MY, Isberg RR. LnaB: a Legionella pneumophila activator of NF-kappaB. Cell. Microbiol. 12(8), 1083-1097 (2010).
    • (2010) Cell. Microbiol. , vol.12 , Issue.8 , pp. 1083-1097
    • Losick, V.P.1    Haenssler, E.2    Moy, M.Y.3    Isberg, R.R.4
  • 75
    • 79955585865 scopus 로고    scopus 로고
    • Protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila
    • Hervet E, Charpentier X, Vianney A et al. Protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila. Infect. Immun. 79(5), 1936-1950 (2011).
    • (2011) Infect. Immun. , vol.79 , Issue.5 , pp. 1936-1950
    • Hervet, E.1    Charpentier, X.2    Vianney, A.3
  • 76
    • 83655174194 scopus 로고    scopus 로고
    • Control of host cell phosphorylation by Legionella pneumophila
    • Comprehensive review on how Legionella pneumophila controls host functions through phosphorylation of host proteins
    • Haenssler E, Isberg RR. Control of host cell phosphorylation by Legionella pneumophila. Front. Microbiol. 2, 64 (2011). Comprehensive review on how Legionella pneumophila controls host functions through phosphorylation of host proteins.
    • (2011) Front. Microbiol. , vol.2 , pp. 64
    • Haenssler, E.1    Isberg, R.R.2
  • 78
    • 42749095602 scopus 로고    scopus 로고
    • Structure and mode of action of clostridial glucosylating toxins: The ABCD model
    • Jank T, Aktories K. Structure and mode of action of clostridial glucosylating toxins: the ABCD model. Trends Microbiol. 16(5), 222-229 (2008).
    • (2008) Trends Microbiol. , vol.16 , Issue.5 , pp. 222-229
    • Jank, T.1    Aktories, K.2
  • 79
    • 0037222925 scopus 로고    scopus 로고
    • Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila
    • Belyi I, Popoff MR, Cianciotto NP. Purification and characterization of a UDP-glucosyltransferase produced by Legionella pneumophila. Infect. Immun. 71(1), 181-186 (2003).
    • (2003) Infect. Immun. , vol.71 , Issue.1 , pp. 181-186
    • Belyi, I.1    Popoff, M.R.2    Cianciotto, N.P.3
  • 80
    • 33750944019 scopus 로고    scopus 로고
    • Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A
    • Belyi Y, Niggeweg R, Opitz B et al. Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A. Proc. Natl Acad. Sci. USA 103(45), 16953-16958 (2006).
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , Issue.45 , pp. 16953-16958
    • Belyi, Y.1    Niggeweg, R.2    Opitz, B.3
  • 81
    • 77954377942 scopus 로고    scopus 로고
    • EEF1A: Thinking outside the ribosome
    • Mateyak MK, Kinzy TG. eEF1A: thinking outside the ribosome. J. Biol. Chem. 285(28), 21209-21213 (2010).
    • (2010) J. Biol. Chem. , vol.285 , Issue.28 , pp. 21209-21213
    • Mateyak, M.K.1    Kinzy, T.G.2
  • 82
    • 79959213985 scopus 로고    scopus 로고
    • Bacterial protein toxins that modify host regulatory GTPases
    • Aktories K. Bacterial protein toxins that modify host regulatory GTPases. Nat. Rev. Microbiol. 9(7), 487-498 (2011).
    • (2011) Nat. Rev. Microbiol. , vol.9 , Issue.7 , pp. 487-498
    • Aktories, K.1
  • 83
    • 41949084350 scopus 로고    scopus 로고
    • Lgt: A family of cytotoxic glucosyltransferases produced by Legionella pneumophila
    • Belyi Y, Tabakova I, Stahl M, Aktories K. Lgt: a family of cytotoxic glucosyltransferases produced by Legionella pneumophila. J. Bacteriol. 190(8), 3026-3035 (2008).
    • (2008) J. Bacteriol. , vol.190 , Issue.8 , pp. 3026-3035
    • Belyi, Y.1    Tabakova, I.2    Stahl, M.3    Aktories, K.4
  • 84
    • 65549084822 scopus 로고    scopus 로고
    • Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response
    • Shen X, Banga S, Liu Y et al. Targeting eEF1A by a Legionella pneumophila effector leads to inhibition of protein synthesis and induction of host stress response. Cell. Microbiol. 11(6), 911-926 (2009).
    • (2009) Cell. Microbiol. , vol.11 , Issue.6 , pp. 911-926
    • Shen, X.1    Banga, S.2    Liu, Y.3
  • 85
    • 79952203418 scopus 로고    scopus 로고
    • Secreted bacterial effectors that inhibit host protein synthesis are critical for induction of the innate immune response to virulent Legionella pneumophila
    • Fontana MF, Banga S, Barry KC et al. Secreted bacterial effectors that inhibit host protein synthesis are critical for induction of the innate immune response to virulent Legionella pneumophila. PLoS Pathog. 7(2), E1001289 (2011).
    • (2011) PLoS Pathog. , vol.7 , Issue.2
    • Fontana, M.F.1    Banga, S.2    Barry, K.C.3
  • 86
    • 83755222623 scopus 로고    scopus 로고
    • Innate immunity to Legionella pneumophila
    • Massis LM, Zamboni DS. Innate immunity to Legionella pneumophila. Front. Microbiol. 2, 109 (2011).
    • (2011) Front. Microbiol. , vol.2 , pp. 109
    • Massis, L.M.1    Zamboni, D.S.2
  • 87
    • 84055202984 scopus 로고    scopus 로고
    • Effector glycosyltransferases in Legionella
    • Belyi Y, Jank T, Aktories K. Effector glycosyltransferases in Legionella. Front. Microbiol. 2, 76 (2011).
    • (2011) Front. Microbiol. , vol.2 , pp. 76
    • Belyi, Y.1    Jank, T.2    Aktories, K.3
  • 88
    • 63649139064 scopus 로고    scopus 로고
    • The fic domain: Regulation of cell signaling by adenylylation
    • Worby CA, Mattoo S, Kruger RP et al. The fic domain: regulation of cell signaling by adenylylation. Mol. Cell 34(1), 93-103 (2009).
    • (2009) Mol. Cell , vol.34 , Issue.1 , pp. 93-103
    • Worby, C.A.1    Mattoo, S.2    Kruger, R.P.3
  • 89
    • 58149400542 scopus 로고    scopus 로고
    • AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling
    • Yarbrough ML, Li Y, Kinch LN, Grishin NV, Ball HL, Orth K. AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling. Science 323(5911), 269-272 (2009).
    • (2009) Science , vol.323 , Issue.5911 , pp. 269-272
    • Yarbrough, M.L.1    Li, Y.2    Kinch, L.N.3    Grishin, N.V.4    Ball, H.L.5    Orth, K.6
  • 90
    • 66149098151 scopus 로고    scopus 로고
    • Bacterial Fic proteins AMP up infection
    • Comprehensive review on the function of Fic domain proteins of different bacterial pathogens
    • Roy CR, Mukherjee S. Bacterial Fic proteins AMP up infection. Sci. Signal. 2(62), PE14 (2009). Comprehensive review on the function of Fic domain proteins of different bacterial pathogens.
    • (2009) Sci. Signal. , vol.2 , Issue.62
    • Roy, C.R.1    Mukherjee, S.2
  • 91
    • 77955872117 scopus 로고    scopus 로고
    • The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b
    • First report that the L. pneumophila effector DrrA (SidM) has AMPylation activity towards Rab
    • Müller MP, Peters H, Blümer J, Blankenfeldt W, Goody RS, Itzen A. The Legionella effector protein DrrA AMPylates the membrane traffic regulator Rab1b. Science 329(5994), 946-949 (2010). First report that the L. pneumophila effector DrrA (SidM) has AMPylation activity towards Rab.
    • (2010) Science , vol.329 , Issue.5994 , pp. 946-949
    • Müller, M.P.1    Peters, H.2    Blümer, J.3    Blankenfeldt, W.4    Goody, R.S.5    Itzen, A.6
  • 92
    • 64149084796 scopus 로고    scopus 로고
    • Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila
    • Brombacher E, Urwyler S, Ragaz C et al. Rab1 guanine nucleotide exchange factor SidM is a major phosphatidylinositol 4-phosphate-binding effector protein of Legionella pneumophila. J. Biol. Chem. 284(8), 4846-4856 (2009).
    • (2009) J. Biol. Chem. , vol.284 , Issue.8 , pp. 4846-4856
    • Brombacher, E.1    Urwyler, S.2    Ragaz, C.3
  • 93
    • 0030920782 scopus 로고    scopus 로고
    • G protein mechanisms: Insights from structural analysis
    • Sprang SR. G protein mechanisms: insights from structural analysis. Annu. Rev. Biochem. 66, 639-678 (1997).
    • (1997) Annu. Rev. Biochem. , vol.66 , pp. 639-678
    • Sprang, S.R.1
  • 94
    • 36249027095 scopus 로고    scopus 로고
    • Legionella pneumophila proteins that regulate Rab1 membrane cycling
    • Demonstrates that DrrA (SidM) of L. pneumophila functions as both a GDP-dissociation inhibitor-displacement factor and a nucleotide exchange factor for Rab
    • Ingmundson A, Delprato A, Lambright DG, Roy CR. Legionella pneumophila proteins that regulate Rab1 membrane cycling. Nature 450(7168), 365-369 (2007). Demonstrates that DrrA (SidM) of L. pneumophila functions as both a GDP-dissociation inhibitor-displacement factor and a nucleotide exchange factor for Rab.
    • (2007) Nature , vol.450 , Issue.7168 , pp. 365-369
    • Ingmundson, A.1    Delprato, A.2    Lambright, D.G.3    Roy, C.R.4
  • 95
    • 84889234796 scopus 로고    scopus 로고
    • A bifunctional bacterial protein links GDI displacement to Rab1 activation
    • Demonstrates that DrrA (SidM) of L. pneumophila functions as both a GDI-displacement factor and a nucleotide exchange factor for Rab
    • Machner MP, Isberg RR. A bifunctional bacterial protein links GDI displacement to Rab1 activation. Science 318(5852), 974-977 (2007). Demonstrates that DrrA (SidM) of L. pneumophila functions as both a GDI-displacement factor and a nucleotide exchange factor for Rab.
    • (2007) Science , vol.318 , Issue.5852 , pp. 974-977
    • Machner, M.P.1    Isberg, R.R.2
  • 96
    • 72449132474 scopus 로고    scopus 로고
    • RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity
    • Schoebel S, Oesterlin LK, Blankenfeldt W, Goody RS, Itzen A. RabGDI displacement by DrrA from Legionella is a consequence of its guanine nucleotide exchange activity. Mol. Cell 36(6), 1060-1072 (2009).
    • (2009) Mol. Cell , vol.36 , Issue.6 , pp. 1060-1072
    • Schoebel, S.1    Oesterlin, L.K.2    Blankenfeldt, W.3    Goody, R.S.4    Itzen, A.5
  • 97
    • 79960699136 scopus 로고    scopus 로고
    • De-AMPylation of the small GTPase Rab1 by the Pathogen Legionella pneumophila
    • First description of a L. pneumophila effector that encodes de-AMPylation activity towards Rab
    • Neunuebel MR, Chen Y, Gaspar AH, Backlund PS Jr, Yergey A, Machner MP. De-AMPylation of the small GTPase Rab1 by the Pathogen Legionella pneumophila. Science 333(6041), 453-456 (2011). First description of a L. pneumophila effector that encodes de-AMPylation activity towards Rab.
    • (2011) Science , vol.333 , Issue.6041 , pp. 453-456
    • Neunuebel, M.R.1    Chen, Y.2    Gaspar, A.H.3    Backlund Jr., P.S.4    Yergey, A.5    Machner, M.P.6
  • 98
    • 79960929331 scopus 로고    scopus 로고
    • Legionella pneumophila SidD is a deAMPylase that modifies Rab1
    • First description of a L. pneumophila effector that encodes de-AMPylation activity towards Rab
    • Tan Y, Luo ZQ. Legionella pneumophila SidD is a deAMPylase that modifies Rab1. Nature 475(7357), 506-509 (2011). First description of a L. pneumophila effector that encodes de-AMPylation activity towards Rab.
    • (2011) Nature , vol.475 , Issue.7357 , pp. 506-509
    • Tan, Y.1    Luo, Z.Q.2
  • 99
    • 2442537071 scopus 로고    scopus 로고
    • Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle
    • Kagan JC, Stein MP, Pypaert M, Roy CR. Legionella subvert the functions of Rab1 and Sec22b to create a replicative organelle. J. Exp. Med. 199(9), 1201-1211 (2004).
    • (2004) J. Exp. Med. , vol.199 , Issue.9 , pp. 1201-1211
    • Kagan, J.C.1    Stein, M.P.2    Pypaert, M.3    Roy, C.R.4
  • 100
    • 2142758690 scopus 로고    scopus 로고
    • Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system
    • Derré I, Isberg RR. Legionella pneumophila replication vacuole formation involves rapid recruitment of proteins of the early secretory system. Infect. Immun. 72(5), 3048-3053 (2004).
    • (2004) Infect. Immun. , vol.72 , Issue.5 , pp. 3048-3053
    • Derré, I.1    Isberg, R.R.2
  • 101
    • 80052271972 scopus 로고    scopus 로고
    • Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD
    • Rigden DJ. Identification and modelling of a PPM protein phosphatase fold in the Legionella pneumophila deAMPylase SidD. FEBS Lett. 585(17), 2749-2754 (2011).
    • (2011) FEBS Lett. , vol.585 , Issue.17 , pp. 2749-2754
    • Rigden, D.J.1
  • 102
    • 67149136177 scopus 로고    scopus 로고
    • Fido, a novel AMPylation domain common to fic, doc, and AvrB
    • Kinch LN, Yarbrough ML, Orth K, Grishin NV. Fido, a novel AMPylation domain common to fic, doc, and AvrB. PLoS One 4(6), E5818 (2009).
    • (2009) PLoS One , vol.4 , Issue.6
    • Kinch, L.N.1    Yarbrough, M.L.2    Orth, K.3    Grishin, N.V.4
  • 103
    • 0025861991 scopus 로고
    • Functional analysis of the fic gene involved in regulation of cell division
    • Komano T, Utsumi R, Kawamukai M. Functional analysis of the fic gene involved in regulation of cell division. Res. Microbiol. 142(2-3), 269-277 (1991).
    • (1991) Res. Microbiol. , vol.142 , Issue.2-3 , pp. 269-277
    • Komano, T.1    Utsumi, R.2    Kawamukai, M.3
  • 104
    • 77951248403 scopus 로고    scopus 로고
    • Histophilus somni IbpA DR2/Fic in virulence and immunoprotection at the natural host alveolar epithelial barrier
    • Zekarias B, Mattoo S, Worby C, Lehmann J, Rosenbusch RF, Corbeil LB. Histophilus somni IbpA DR2/Fic in virulence and immunoprotection at the natural host alveolar epithelial barrier. Infect. Immun. 78(5), 1850-1858 (2010).
    • (2010) Infect. Immun. , vol.78 , Issue.5 , pp. 1850-1858
    • Zekarias, B.1    Mattoo, S.2    Worby, C.3    Lehmann, J.4    Rosenbusch, R.F.5    Corbeil, L.B.6
  • 105
    • 79952128780 scopus 로고    scopus 로고
    • Fic domain-catalyzed adenylylation: Insight provided by the structural analysis of the type IV secretion system effector BepA
    • Palanivelu DV, Goepfert A, Meury M, Guye P, Dehio C, Schirmer T. Fic domain-catalyzed adenylylation: insight provided by the structural analysis of the type IV secretion system effector BepA. Protein Sci. 20(3), 492-499 (2011).
    • (2011) Protein Sci. , vol.20 , Issue.3 , pp. 492-499
    • Palanivelu, D.V.1    Goepfert, A.2    Meury, M.3    Guye, P.4    Dehio, C.5    Schirmer, T.6
  • 106
    • 46249111623 scopus 로고    scopus 로고
    • Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors
    • Analysis of ankyrin motif proteins of L. pneumophila and Coxiella burnetti showing that they are secreted bacterial effectors that modulate host cell functions
    • Pan X, Lührmann A, Satoh A, Laskowski-Arce MA, Roy CR. Ankyrin repeat proteins comprise a diverse family of bacterial type IV effectors. Science 320(5883), 1651-1654 (2008). Analysis of ankyrin motif proteins of L. pneumophila and Coxiella burnetti showing that they are secreted bacterial effectors that modulate host cell functions.
    • (2008) Science , vol.320 , Issue.5883 , pp. 1651-1654
    • Pan, X.1    Lührmann, A.2    Satoh, A.3    Laskowski-Arce, M.A.4    Roy, C.R.5
  • 107
    • 80052399642 scopus 로고    scopus 로고
    • Modulation of Rab GTPase function by a protein phosphocholine transferase
    • Describes for the first time phosphocholination of Rab by a bacterial effector
    • Mukherjee S, Liu X, Arasaki K, Mcdonough J, Galán JE, Roy CR. Modulation of Rab GTPase function by a protein phosphocholine transferase. Nature 477(7362), 103-106 (2011). Describes for the first time phosphocholination of Rab by a bacterial effector.
    • (2011) Nature , vol.477 , Issue.7362 , pp. 103-106
    • Mukherjee, S.1    Liu, X.2    Arasaki, K.3    Mcdonough, J.4    Galán, J.E.5    Roy, C.R.6
  • 108
    • 84855504174 scopus 로고    scopus 로고
    • Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination
    • Describes for the first time the dephosphorylcholinate activity of a bacterial effector
    • Tan Y, Arnold RJ, Luo ZQ. Legionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholination. Proc. Natl Acad. Sci. USA 108(52), 21212-21217 (2011). Describes for the first time the dephosphorylcholinate activity of a bacterial effector.
    • (2011) Proc. Natl Acad. Sci. USA , vol.108 , Issue.52 , pp. 21212-21217
    • Tan, Y.1    Arnold, R.J.2    Luo, Z.Q.3
  • 109
    • 84858067652 scopus 로고    scopus 로고
    • Bacterial effector-involved temporal and spatial regulation by hijack of the host ubiquitin pathway
    • Kubori T, Nagai A. Bacterial effector-involved temporal and spatial regulation by hijack of the host ubiquitin pathway. Front. Microbiol. 2, 145 (2011).
    • (2011) Front. Microbiol. , vol.2 , pp. 145
    • Kubori, T.1    Nagai, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.